ID W1S6E5_9SPHN Unreviewed; 348 AA.
AC W1S6E5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Extracellular exo-alpha-(1->5)-L-arabinofuranosidase {ECO:0000256|PIRNR:PIRNR026534};
DE EC=3.2.1.55 {ECO:0000256|PIRNR:PIRNR026534};
GN ORFNames=C100_11735 {ECO:0000313|EMBL:ETI63589.1};
OS Sphingobium sp. C100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1207055 {ECO:0000313|EMBL:ETI63589.1, ECO:0000313|Proteomes:UP000018867};
RN [1] {ECO:0000313|EMBL:ETI63589.1, ECO:0000313|Proteomes:UP000018867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C100 {ECO:0000313|EMBL:ETI63589.1,
RC ECO:0000313|Proteomes:UP000018867};
RX PubMed=24482512;
RA Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.;
RT "Draft Genome Sequence of Sphingobium sp. Strain C100, a Polycyclic
RT Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of the
RT Arctic Ocean.";
RL Genome Announc. 2:0-0(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000256|PIRNR:PIRNR026534};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834, ECO:0000256|PIRNR:PIRNR026534}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|PIRNR:PIRNR026534}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETI63589.1}.
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DR EMBL; AYOY01000145; ETI63589.1; -; Genomic_DNA.
DR RefSeq; WP_024019979.1; NZ_AYOY01000145.1.
DR AlphaFoldDB; W1S6E5; -.
DR STRING; 1207055.C100_11735; -.
DR PATRIC; fig|1207055.3.peg.2215; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR UniPathway; UPA00667; -.
DR Proteomes; UP000018867; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:InterPro.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd08998; GH43_Arb43a-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW Reference proteome {ECO:0000313|Proteomes:UP000018867};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..348
FT /note="Extracellular exo-alpha-(1->5)-L-
FT arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004809085"
FT REGION 198..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT ACT_SITE 224
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 163..166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT BINDING 183..185
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT SITE 166
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-3"
FT SITE 298
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000256|PIRSR:PIRSR026534-3"
SQ SEQUENCE 348 AA; 38227 MW; 796E8F2D14970C7B CRC64;
MKRHIIATFP VLALLIGAAC AQQPAEPPRG TLNSRLTGDL VPTHDPVIIR QGDIYHVFST
GHGKRLIETR TSPDLVHWTA GDPVFTALPD WATKAIPGSN GIWAPDISYV NGRYRLYYSV
STFGSNRSAI GLATSPTLDP KAPDFGWRDE GLVVMSTKDD DYNAIDPNFI IDRDGRHWLT
LGSFWTGIKL FELDPKTGKP KDPKAKPLSI ARRPAPAGGP APVEAPFIID HGGYYWLMVS
YDYCCKGVNS SYYTVIGRSK DITGPYLGKD GSKLMEGGGT IFIRADLQEQ QRWRGPGHAG
WLHDVDGKNG DGRDYVVYHA YDKQADGAPT LRIAPVTWGA DGWPQADY
//
